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Database: UniProt/TrEMBL
Entry: A2C0L0_PROM1
LinkDB: A2C0L0_PROM1
Original site: A2C0L0_PROM1 
ID   A2C0L0_PROM1            Unreviewed;       456 AA.
AC   A2C0L0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   25-OCT-2017, entry version 72.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   Name=pdhC {ECO:0000313|EMBL:ABM75020.1};
GN   OrderedLocusNames=NATL1_04561 {ECO:0000313|EMBL:ABM75020.1};
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555 {ECO:0000313|EMBL:ABM75020.1, ECO:0000313|Proteomes:UP000002592};
RN   [1] {ECO:0000313|Proteomes:UP000002592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A {ECO:0000313|Proteomes:UP000002592};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA   Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA   Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; CP000553; ABM75020.1; -; Genomic_DNA.
DR   RefSeq; WP_011823207.1; NC_008819.1.
DR   ProteinModelPortal; A2C0L0; -.
DR   STRING; 167555.NATL1_04561; -.
DR   EnsemblBacteria; ABM75020; ABM75020; NATL1_04561.
DR   KEGG; pme:NATL1_04561; -.
DR   eggNOG; ENOG4107UKP; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H04EL; -.
DR   Proteomes; UP000002592; Chromosome.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR004167; E3-bd.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ABM75020.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002592};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ABM75020.1}.
FT   DOMAIN        3     81       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   456 AA;  48224 MW;  8BC52E9DE546F9DB CRC64;
     MATHDIFMPA LSSTMTEGKI VEWLKKPGDK VERGESVLVV ESDKADMDVE SFQDGFLASI
     VMPAGSSAPV GETIGLIVET EDEIAAAQAN SPSPSPQSGS QEKDSSSPQV QEKQASVDSP
     KATVVTKASP APLVSESSVN QDQFLNDGRI VASPRAKKLA SQMGVDLATV RGSGPHGRIQ
     AEDVQSAKGQ PISVPWIAES NAPAKIVSDV PRVEKKSVDA GKPPAPGKSF GSRGETIAFN
     TLQQAVNRNM EESLNTPCFR VGYSILTDEL DDLYKQVKPD GVTMTALLAK AVGLTLARHP
     QVNAAFSSEG IAYPSQINVA VAVAMEDGGL ITPVLQNADK TSLTDLSLQW ADLVKRARNK
     QLEPQEYSSG TFTLSNLGMF GVDRFDAILP PGTGAILAVG ASLSKVVASK DGSISIKKQM
     QVNLTADHRV IYGADGALFL KDLAYLIEKN PYSLSS
//
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